MBOA2_RAT
ID MBOA2_RAT Reviewed; 519 AA.
AC Q3T1J2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lysophospholipid acyltransferase 2 {ECO:0000250|UniProtKB:Q6ZWT7};
DE Short=LPLAT 2;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=1-acylglycerophosphate O-acyltransferase;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase {ECO:0000250|UniProtKB:Q6ZWT7};
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase {ECO:0000250|UniProtKB:Q6ZWT7};
DE EC=2.3.1.n7 {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
DE Short=Lyso-PA acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 4;
DE Short=Lyso-PC acyltransferase 4;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE Short=LPEAT;
DE Short=Lyso-PE acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2;
DE Short=O-acyltransferase domain-containing protein 2;
GN Name=Mboat2 {ECO:0000312|RGD:1305798}; Synonyms=Oact2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC group from an acyl-CoA to a lysophospholipid leading to the production
CC of a phospholipid and participates in the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle. May
CC catalyze preferentially the acylation of lysophosphatidylethanolamine
CC (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) and lysophosphatidic
CC acid (LPA) and to a lesser extend lysophosphatidylcholine (LPC) and
CC lysophosphatidylserine (LPS). Prefers oleoyl-CoA as the acyl donor (By
CC similarity). May be involved in chondrocyte differentiation (By
CC similarity). {ECO:0000250|UniProtKB:Q6ZWT7,
CC ECO:0000250|UniProtKB:Q8R3I2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:36015, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36016;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z)-hexadecenoyl-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37419, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73004, ChEBI:CHEBI:73999;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37420;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine +
CC hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-
CC phosphoserine + CoA; Xref=Rhea:RHEA:37415, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:74617, ChEBI:CHEBI:74909;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37416;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-[(9Z)-hexadec-9-enoyl]-sn-glycero-3-phosphate +
CC CoA; Xref=Rhea:RHEA:37223, ChEBI:CHEBI:57287, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73998;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37224;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphocholine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37627, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:77287, ChEBI:CHEBI:77294;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37628;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37631,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:77288,
CC ChEBI:CHEBI:77291; Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37523, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75036, ChEBI:CHEBI:75038;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37524;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphocholine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37519, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37520;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- ACTIVITY REGULATION: Partially inhibited by thimerosal.
CC {ECO:0000250|UniProtKB:Q6ZWT7}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:Q6ZWT7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6ZWT7}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q6ZWT7}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q8R3I2}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC101889; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03049793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03054282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03052483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03050975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03049616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101889; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001101486.2; NM_001108016.2.
DR AlphaFoldDB; Q3T1J2; -.
DR SMR; Q3T1J2; -.
DR STRING; 10116.ENSRNOP00000009018; -.
DR PaxDb; Q3T1J2; -.
DR PRIDE; Q3T1J2; -.
DR Ensembl; ENSRNOT00000082657; ENSRNOP00000075292; ENSRNOG00000061050.
DR GeneID; 313997; -.
DR KEGG; rno:313997; -.
DR CTD; 129642; -.
DR RGD; 1305798; Mboat2.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; Q3T1J2; -.
DR OMA; WAISIFE; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q3T1J2; -.
DR TreeFam; TF314906; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q3T1J2; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000061050; Expressed in esophagus and 16 other tissues.
DR Genevisible; Q3T1J2; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..519
FT /note="Lysophospholipid acyltransferase 2"
FT /id="PRO_0000273022"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 341
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /evidence="ECO:0000250"
SQ SEQUENCE 519 AA; 59001 MW; D5CAFBD16F7642B3 CRC64;
MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA
TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMHQ CCFVFALGYL SVCQITRVYI
FDYGQYSADF SGPMMIITQK ITSLAYEIHD GMFRKDEELT PSQRGLAVRR MPSLLEYVSY
TCNFMGILAG PLCSYKDYIA FIEGRASHMA QSGENGKEEQ HGKAEPSPNA AVTEKLLVCG
LSLLFHLTIS SMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA
AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR VCYERATFSP
TVQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR HYFVEPPQLK LFYDIITWAA
TQITISYTVV PFVLLSINPS FTFYRSWYYC LHICSILVLL LLPVKKSPRK KNTEENAQPS
WAKKFDEREN SLGQNSFSMM NNVCNQNQDT GSRHSALTQ
